Abstract
Surface plasmon resonance (SPR)/BIAcore technology enables the characterization of molecular interactions, including determination of affinities and kinetics. In BIAcore, one of the interaction partners (the ligand) is immobilized on a chip and the other (the analyte) is provided in solution. BIAcore allows to study association and dissociation rates in real time without the use of labeling. BIAcore can be applied to molecular interactions involving small compounds and biological macromolecules such as proteins, lipids, nucleic acids, or carbohydrates. Here we describe protocols for the measurements of PDZ domain–peptide (oriented biotinylated peptides), PDZ domain–liposomes (lipid membranes), and PDZ–lipid–peptide tripartite interactions.
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Acknowledgments
Work in the laboratory of PZ is currently supported by the Fund for Scientific Research–Flanders (FWO Grants G.0846.15 and G0C5718N), the Agence Nationale de la Recherche (ANR-18-CE13-0017, Project SynTEV) and receives funding from the European Union’s Horizon 2020 research and innovation program under the Marie Sklodowska-Curie grant agreement no. 747025.
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Zimmermann, P., Egea-Jimenez, A.L. (2021). Study of PDZ–Peptide and PDZ–Lipid Interactions by Surface Plasmon Resonance/BIAcore. In: Borg, JP. (eds) PDZ Mediated Interactions. Methods in Molecular Biology, vol 2256. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1166-1_5
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DOI: https://doi.org/10.1007/978-1-0716-1166-1_5
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